CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009505
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras-related protein Rab-11A 
Protein Synonyms/Alias
 Rab-11; YL8 
Gene Name
 RAB11A 
Gene Synonyms/Alias
 RAB11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24IGDSGVGKSNLLSRFubiquitination[1, 2]
61QVDGKTIKAQIWDTAubiquitination[1, 2]
95LLVYDIAKHLTYENVubiquitination[2]
107ENVERWLKELRDHADubiquitination[2]
179IYRIVSQKQMSDRREubiquitination[1, 2, 3, 4]
207VPPTTENKPKVQCCQubiquitination[3, 5]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048
Functional Description
 The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes. 
Sequence Annotation
 NP_BIND 18 26 GTP.
 NP_BIND 66 70 GTP.
 NP_BIND 124 127 GTP.
 NP_BIND 154 156 GTP.
 MOTIF 40 48 Effector region (By similarity).
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 213 213 Cysteine methyl ester (Potential).
 LIPID 212 212 S-geranylgeranyl cysteine (By
 LIPID 213 213 S-geranylgeranyl cysteine (By  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell membrane; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Endosome; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 216 AA 
Protein Sequence
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI 60
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM 120
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ 180
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI 216 
Gene Ontology
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
 GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0055037; C:recycling endosome; ISS:UniProtKB.
 GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005802; C:trans-Golgi network; IDA:MGI.
 GO:0030133; C:transport vesicle; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IDA:UniProtKB.
 GO:0019905; F:syntaxin binding; NAS:UniProtKB.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0032402; P:melanosome transport; ISS:UniProtKB.
 GO:0031175; P:neuron projection development; IMP:UniProtKB.
 GO:0048227; P:plasma membrane to endosome transport; NAS:UniProtKB.
 GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Compara.
 GO:0051223; P:regulation of protein transport; IEA:Compara.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0006833; P:water transport; TAS:Reactome. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR003579; Small_GTPase_Rab_type. 
Pfam
 PF00071; Ras 
SMART
 SM00175; RAB 
PROSITE
 PS51419; RAB 
PRINTS
 PR00449; RASTRNSFRMNG.